GLORIA

GEOMAR Library Ocean Research Information Access

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Online Resource
    Online Resource
    Paris :Springer Paris,
    Keywords: Neovascularization. ; Electronic books.
    Description / Table of Contents: This book reviews recent advances in understanding of the molecular and cellular mechanisms of angiogenesis, with a focus on how to integrate these observations into the context of developmental, post-natal and pathological neovascularization.
    Type of Medium: Online Resource
    Pages: 1 online resource (501 pages)
    Edition: 1st ed.
    ISBN: 9782817804668
    DDC: 612.13
    Language: English
    Note: Intro -- Contents -- Angiogenesis: An Ever-Challenging Research Field -- Acknowledgment -- References -- Part I: Angiogenesis During Embryonic Development -- Chapter 1: Emergence of Endothelial Cells During Vascular Development -- 1.1 Introduction -- 1.2 Vasculogenesis -- 1.3 Hemangioblast -- 1.4 Remodeling of the Primary Capillary Plexus into Arteries and Veins -- 1.5 Role of Hemodynamic Forces in Remodeling -- 1.6 Guidance of Capillaries by Endothelial Tip Cells -- 1.7 Circulating Endothelial Cells in the Embryo -- 1.8 Perspectives -- References -- Chapter 2: Lymphatic Vascular Morphogenesis -- 2.1 Early Steps of Lymphatic Vascular Development -- 2.1.1 Lymphatic Endothelial Cell Specification -- 2.1.2 Lymphatic Vessel Sprouting from the Veins -- 2.1.3 Separation of Lymphatic and Blood Vasculatures -- 2.1.4 Non-venous Origins of Lymphatic Vasculature -- 2.2 Lymphatic Vessel Remodelling -- 2.2.1 Sprouting and Growth of Lymphatic Vessels -- 2.2.2 Regulation of Lymphatic Endothelial Cell-Cell Junctions -- 2.2.3 Valve Morphogenesis -- 2.2.4 Smooth Muscle Cells Recruitment to Collecting Lymphatic Vessels -- 2.3 Lymphatic Vasculature and Diseases -- 2.3.1 Lymphoedema -- 2.3.2 Inflammation -- 2.3.3 Tumour Metastasis -- 2.3.4 Lipid Absorption -- 2.4 Concluding Remarks -- References -- Part II: The Physiological Angiogenic Signal: Cellular and Molecular Mechanisms -- Chapter 3: Finding New Partnerships: The Function of Individual Extracellular Receptor Domains in Angiogenic Signalling by VEGF Receptors -- 3.1 Biology of VEGF Family Growth Factors and Their Receptors -- 3.1.1 Introduction to VEGF -- 3.1.2 Structure-Function Relationship of VEGF and VEGF Receptors -- 3.1.2.1 Receptor Specificity of VEGFs -- 3.1.2.2 Structural Analysis of VEGF Binding to VEGFR-1, VEGFR-2 and VEGFR-3 -- 3.1.2.3 Activation of VEGF Receptors. , 3.2 VEGFR-2 as Part of a Signalling Platform -- 3.2.1 Neuropilins (NRPs) -- 3.2.2 Ephrin-B2 -- 3.2.3 VE-Cadherin -- 3.2.4 Dopamine Receptor D2 -- 3.2.5 CD146 -- 3.2.6 CD44 -- 3.3 Extracellular Components of the VEGF/VEGFR Signalling Cascade as Targets for Therapy and Functional Inhibition -- 3.3.1 VEGF/VEGFRs in Disease -- 3.3.2 VEGF/VEGFRs as Targets in Therapeutic Inhibition -- 3.3.2.1 VEGF-Neutralising Agents -- 3.3.2.2 Anti-VEGFR-1 Agents -- 3.3.2.3 Anti-VEGFR-2 D23 Agents -- 3.3.2.4 Anti-VEGFR-2 D4-7 Agents -- 3.3.3 Limitations to VEGF/VEGFR Targeted Therapy -- 3.3.4 Outlook and Conclusions -- References -- Chapter 4: Wnt/Frizzled Signaling in the Vasculature -- 4.1 Introduction -- 4.1.1 Wnt Signal Transduction -- 4.1.1.1 The Canonical Pathway: Wnt/β-Catenin -- 4.1.1.2 The Planar Cell Polarity Pathway -- 4.1.1.3 The Calcium-Mediated Pathway -- 4.1.2 Wnt Inhibitors and Modulators -- 4.1.3 Atypical Receptors Kinases -- 4.2 Role of the Wnt/Frizzled in Vascular Development -- 4.2.1 Evidence of Wnt/Fzd Expression and Signaling in Endothelial Cells -- 4.2.2 Placental Development -- 4.2.3 Postnatal Retinal Angiogenesis -- 4.2.4 Brain Vasculature -- 4.3 Role of Wnt Regulation in Vascular Pathology -- 4.3.1 Choroidal Neovascularization and Oxygen-Induced Retinopathy -- 4.3.2 Wound Healing -- 4.3.3 Hind Limb and Cardiac Ischemia -- 4.4 Conclusion -- 4.5 Online Databases -- References -- Chapter 5: BMP9, BMP10, and ALK1: An Emerging Vascular Signaling Pathway with Therapeutic Applications -- 5.1 Bone Morphogenetic Proteins (BMPs) -- 5.2 BMP9/BMP10/ALK1 Signaling Complex -- 5.3 The Role of BMP9 and BMP10 in Vascular Development -- 5.3.1 Knowledge from Human Vascular Diseases -- 5.3.2 Knowledge from Animal Models: Mice and Zebrafish -- 5.3.2.1 Mice -- 5.3.2.2 Zebrafish -- 5.3.3 In Vitro Roles of BMP9 and BMP10 in Endothelial Cells. , 5.4 Therapeutic Applications of the BMP9/BMP10/ALK1 Signaling Pathway -- 5.4.1 HHT -- 5.4.2 BMP9, BMP10, and ALK1 as Biomarkers in Cancer -- 5.4.3 Therapeutic Applications of the BMP9/BMP10/ALK1 Signaling Pathway in Tumor Angiogenesis -- 5.4.3.1 ALK1 Extracellular Domain (ALK1 ECD) -- 5.4.3.2 Anti-ALK1 Antibody (PF-03446962) -- 5.4.3.3 Anti-endoglin Antibody (TRC105) -- 5.5 Conclusions and Perspectives -- References -- Chapter 6: Apelin Signaling in Retinal Angiogenesis -- 6.1 Apelin Signaling -- 6.1.1 Receptor Discovery and Isolation of the Endogenous Ligand -- 6.1.2 Multiple Active Ligands and Receptor Heterodimers -- 6.1.3 Gene Transcription and Mode of Signaling -- 6.1.4 Physiological Functions of Apelin Signaling -- 6.2 The Retina -- 6.2.1 Anatomy and Development -- 6.2.2 Astrocyte: The Key Mediator of Neuron/Endothelial Cell Interactions -- 6.2.3 Developmental Patterning of Retinal Vessels -- 6.2.4 Subpopulations of Endothelial Cells -- 6.3 Apelin Signaling and Formation of Retinal Vessels -- 6.3.1 Apelin: A Bona Fide Angiogenic Factor -- 6.3.2 Vascular Phenotype of Apelin or APJ Gene Invalidation -- 6.3.3 Temporal Expression of Apelin Signaling Coincides with the Angiogenic Phase -- 6.3.4 Apelin Receptor Gene: An Early Marker of the Venous Phenotype -- 6.3.5 Receptor and Ligand Gene as Potential Markers of Tip or Stalk Phenotype -- 6.3.6 Apelin Signaling as a Linker Between VEGF-Secreting Astrocytes and Proliferating Stalk Cells -- 6.3.7 Apelin Signaling Regulates LIF Secretion and Controls Astrocyte Maturation -- 6.4 Apelin Signaling and Pathological Retinal Angiogenesis -- 6.4.1 The Retinopathy of Prematurity -- 6.4.2 Diabetic Retinopathy -- 6.4.3 Telangiectatic Vessels -- 6.5 Clinical Implications -- References -- Chapter 7: Emerging Role of the Two Related Basic Helix-Loop-Helix Proteins TAL1 and LYL1 in Angiogenesis -- 7.1 Introduction. , 7.2 Properties of LYL1 and TAL1 -- 7.3 Hematopoietic Functions of Tal1, Lyl1, and Lmo2 -- 7.4 Tal1 and Lmo2 Are Required for Cardiovascular Development -- 7.5 TAL1 Activity Is Required in the Early Steps of Angiogenesis -- 7.5.1 TAL1 and LMO2 Initiate Tubulogenesis Through VE-Cadherin Upregulation -- 7.5.2 TAL1-LMO2 Complexes Controls Angiopoietin-2 Expression -- 7.6 LYL1 Is Required for the Maturation of New Blood Vessels -- 7.6.1 Lyl1 Deficiency Leads to Increased Angiogenic Responses -- 7.6.2 LYL1 Contributes to Vessel Maturation and Stabilization -- 7.7 Coordinated Activity of TAL1 and LYL1 to Regulate Angiogenic Processes -- References -- Part III: Hypoxia, Ischemia and Angiogenesis -- Chapter 8: Hypoxia and Extracellular Matrix Remodeling -- 8.1 Hypoxia Induction of Angiogenesis -- 8.2 Establishment of the Vascular BM -- 8.3 Extracellular Matrix Proteolytic Degradation -- 8.4 Regulation of Hypoxia-Induced Growth Factor Sequestration in the Extracellular Matrix -- 8.5 Matricellular Proteins -- 8.5.1 Group A Thrombospondins -- 8.5.2 Group B Thrombospondins -- 8.6 Conclusion -- References -- Chapter 9: Sphingosine-1-Phosphate in Hypoxic Signaling -- 9.1 Hypoxia Significance and Impact on Clinical Outcome -- 9.2 The Hypoxia-Inducible Factors -- 9.3 Sphingosine 1-Phosphate Metabolism in Cancer -- 9.4 Sphingosine 1-Phosphate Signaling in Hypoxia -- 9.5 Sphingosine 1-Phosphate Signaling as a Target for Anti- hypoxic Strategy -- 9.6 Concluding Remarks -- References -- Chapter 10: Reciprocal Crosstalk Between Angiogenesis and Metabolism -- 10.1 Regulation of Angiogenesis by Oxygen and Metabolism -- 10.1.1 PHDs and HIF: The Molecular Players of Angiogenesis Are Regulated by Oxygen and Metabolic Intermediates -- 10.1.2 Modulators of HIF and PHDs by Nonhypoxic Stimuli -- 10.1.2.1 TCA Cycle and Other Metabolic Intermediates. , 10.1.2.2 Reactive Oxygen Species -- 10.1.3 Modulation of Angiogenesis by Metabolic Regulators -- 10.2 EC Metabolism Impacts Vessel Sprouting -- 10.2.1 EC Survival and Functions Are Dependent on Glycolysis -- 10.2.2 Metabolic Changes During Vascular Sprouting -- 10.3 Regulation of Metabolism by Angiogenesis -- Bibliography -- Chapter 11: Endothelial Progenitor Cells and Cardiovascular Ischemic Diseases: Characterization, Functions, and Potential Clinical Applications -- 11.1 Introduction -- 11.2 Cultured EPC -- 11.3 Recruitment of EPCs to the Ischemic Tissue -- 11.3.1 CXCL12/CXCR4 -- 11.3.2 Integrins and Selectins -- 11.3.3 Hemostatic Partners, Thrombospondin, and Thrombin Interaction with EPCs -- 11.3.4 Other Factors -- 11.4 Mechanisms of EPC-Related Effects on Postischemic Revascularization -- 11.4.1 Differentiation into Endothelial Cells -- 11.4.2 Paracrine Effects -- 11.4.3 Interaction with the Host Environment -- 11.5 EPCs as Diagnostic and Prognostic Tools -- 11.5.1 EPCs as Biomarkers of Cardiovascular Diseases -- 11.5.1.1 EPCs and Cardiovascular Risk Factors -- 11.5.1.2 EPCs and the Prevalence of CVDs -- 11.5.2 Are EPCs a Useful Prognostic Factor for Cardiovascular Diseases? -- 11.6 EPCs as Therapeutic Tools -- 11.6.1 Adult Stem/Progenitor Cells -- 11.6.2 Alternative Sources of EPCs -- 11.6.2.1 Embryonic Stem Cells (ESCs) -- 11.6.2.2 Induced Pluripotent Stem Cells (iPSCs) -- 11.6.2.3 Local Source of Stem/Progenitor Cells -- 11.7 Conclusion -- References -- Part IV: Tumor Angiogenesis -- Chapter 12: Endothelial Cell Reactions to Oxygen: Implications for Cancer -- 12.1 Overview of Oxygen-Mediated Pathways -- 12.2 Hypoxia-Inducible Factors Mediate Cellular Oxygen Signaling -- 12.3 The Function of Prolyl Hydroxylase Domain Proteins and Factor Inhibiting HIF as Oxygen Sensors. , 12.4 Role of Oxygen Signaling in Physiological and Pathophysiological Angiogenesis.
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 737 (1994), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1573-7209
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A temperature-sensitive mutant with a defect in glycoprotein synthesis and a cell cycle (G1)-specific arrest at the nonpermissive temperature (Tenner et al., J. Cell. Physiol., 90:145-160, 1977; Tenner and Scheffler, J. Cell. Physiol., 98:251-266, 1979) was investigated further after a human epidermal growth factor (EGF) receptor gene had been transfected and amplified in these cells. While a temperature shift-up lead to an immediate arrest in the biosynthesis of mature EGF receptor and its appearance on the plasma membrane, the observed turnover of the preexisting receptor was too slow to account for the arrest of DNA synthesis in these mutant cells. Tunicamycin could in fact mimic the effect of a temperature shift on the biosynthesis of EGF receptor, but it did not have the same rapid effect on DNA synthesis and cell cycle progression. These mutants have also been shown to induce a set of stress proteins or glucose-regulated proteins, GRPs (Lee et al., J. Cell. Physiol., 129:277-282, 1986). The question is addressed whether the defect in glycoprotein synthesis is the primary defect and a possible cause of the induction of the GRPs, or whether a more basic defect at the level of the endoplasmic reticulum (ER) is responsible for the complex phenotype of the mutant. Our results argue in favor of a primary defect which indirectly affects N-linked glycosylation of proteins, as well as several other functions associated with the ER. We hypothesize that the defect affects the calcium distribution between ER and cytosol, since the calcium ionophore A23187 has an effect similar to that of a temperature shift.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A temperature-sensitive mutant of Chinese hamster fibroblasts with a defect in glycoprotein synthesis is investigated after transfection and amplification of the gene for the human EGF receptor. We demonstrate that at the nonpermissive temperature a partially glycosylated species of the receptor accumulates in the endoplasmic reticulum. The oligosaccharides present are the high mannose types, since they can be removed completely by treatment with endoglycosidase H. Pulse-chase experiments show that the abnormal species of the receptor cannot be chased to a form that is either resistant to endoglycosidase H, or altered in its mobility on SDS polyacrylamide gels. The abnormal species of the receptor appears within the first hour of a shift to the nonpermissive temperature, and no further changes are observed upon prolonged incubation of cells at 40deg;C. However, after 3-4 hours immunoprecipitations of the receptor yield another protein, which has properties very similar, if not identical, to the glucose-regulated protein GRP78. The induction of this protein at 40deg;C can be suppressed completely with an inhibitor of RNA synthesis, without any effect on the glycosylation defect, or on the accumulation of the EGF receptor in the endoplasmic reticulum.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Adrenocortical differentiated functions are under the control of both endocrine hormones such as ACTH and local factors such as transforming growth factor β (TGFβ) or basic fibroblast growth factor (bFGF). Besides their regulatory actions on the synthesis of corticosteroids, these two classes of factors also exert some important effects on the cellular environment. We have examined here the regulation by ACTH and TGFβ of adrenocortical cell proteoglycan synthesis and secretion. Under basal conditions, adrenocortical cells synthesized and secreted several species of sulfated proteoglycans, 80% of them being recovered in solution in the culture medium. When analyzed by ion exchange chromatography, the cell extracts and the media from cells metabolically labeled with 35S-suifate were found to contain two and three species of radioactive sulfated proteoglycans, respectively. All species were proteoheparan-sulfates. Treatment of adrenocortical cells with TGFβ1 or ACTH resulted in a significant increase of the incorporation of 35S into both secreted and cell-associated proteoglycans. ACTH stimulated more than three times the amount of secreted proteoglycans eluting from DEAE-Trisacryl as peak B, whereas TGFβ preferentially increased the amount of peak C. No important modification of the size of the synthesized proteoglycans was observed. The subpopulation of heparan sulfate proteoglycans capable to bind bFGF was also largely increased after ACTH or TGFβ treatment and paralleled the variation in overall proteoheparan sulfate synthesis. Thus those effects of TGFβ and ACTH on proteoglycan synthesis may participate in an increased ability of adrenocortical cells to bind and respond to bFGF. © 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 8
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We reported previously that transforming growth factor β (TGF-β) does not influence the proliferation of bovine adrenocortical cells but is a very potent inhibitor of their steroidogenic functions (Feige et al.:Journal of Biological Chemistry 262:13491-13495, 1987). In the present study, we addressed the question of whether these cells modify the synthesis of their extracellular matrix (in particular of fibronectin) in response to TGF-β1, similarly to the changes observed in cell types whose growth is modified by this factor (e.g., fibroblasts). Immunofluorescence studies using anti-fibronectin antibodies revealed that TGF-β1, treatment in serum-free medium induced the formation of fibronectin-containing fibrils associated with adrenocortical cells. Metabolic labeling of adrenocortical cells with [35S]-methionine showed that fibronectin synthesis and secretion were highly stimulated by low concentrations of TGF-β1. Half-maximal stimulation was observed for TGF-β1 concentrations in the range of 0.1 to 0.5 ng/ml and maximal stimulation reached 35-fold over control at the concentration of 2 ng/ml. The earlier detectable effect was observed after 8 h of treatment (6-fold stimulation) and the maximal increase was reached after 24 h of treatment. Stimulation of adrenocortical fibronectin synthesis by TGF-β1 appeared to imply a transcriptional event since it was no longer observed in the presence of DRB, a potent inhibitor of RNA polymerases, and because the level of fibronectin mRNA was stimulated under TGF-β1 treatment. Taken together, these results indicate that the increased expression of fibronectin is not closely related to growth-regulatory effects of TGF-β1 since it is also observed in adrenocortical cells, whose proliferation is unaffected by TGF-β1.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...